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Database: PDB
Entry: 1M9I
LinkDB: 1M9I
Original site: 1M9I 
HEADER    LIPID BINDING PROTEIN                   29-JUL-02   1M9I              
TITLE     CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T356D           
TITLE    2 OF ANNEXIN VI                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANNEXIN VI;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LIPOCORTIN VI, P68, P70, PROTEIN III,                       
COMPND   5 CHROMOBINDIN 20, 67 KDA CALELECTRIN, CALPHOBINDIN-II, CPB-           
COMPND   6 II;                                                                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ANX6;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DB334;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: GAL10;                                
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEPDB60                                   
KEYWDS    ANNEXIN, CALCIUM-BINDING, MEMBRANE-BINDING, PHOSPHORYLATION,          
KEYWDS   2 MUTANT T356D, LIPID BINDING PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.FREYE-MINKS,R.H.KRETSINGER,C.E.CREUTZ                               
REVDAT   3   24-FEB-09 1M9I    1       VERSN                                    
REVDAT   2   15-APR-03 1M9I    1       JRNL   REMARK                            
REVDAT   1   07-AUG-02 1M9I    0                                                
JRNL        AUTH   C.FREYE-MINKS,R.H.KRETSINGER,C.E.CREUTZ                      
JRNL        TITL   STRUCTURAL AND DYNAMIC CHANGES IN HUMAN ANNEXIN VI           
JRNL        TITL 2 INDUCED BY A PHOSPHORYLATION-MIMICKING MUTATION,             
JRNL        TITL 3 T356D                                                        
JRNL        REF    BIOCHEMISTRY                  V.  42   620 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12534274                                                     
JRNL        DOI    10.1021/BI026742H                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.BENZ,A.BERGNER,A.HOFMANN,P.DEMANGE,P.GOTTIG,               
REMARK   1  AUTH 2 S.LIEMANN,R.HUBER,D.VOGES                                    
REMARK   1  TITL   THE STRUCTURE OF RECOMBINANT HUMAN ANNEXIN VI IN             
REMARK   1  TITL 2 CRYSTALS AND MEMBRANE-BOUND                                  
REMARK   1  REF    J.MOL.BIOL.                   V. 260   638 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1996.0426                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.J.AVILA-SAKAR,C.E.CREUTZ,R.H.KRETSINGER                    
REMARK   1  TITL   CRYSTAL STRUCTURE OF BOVINE ANNEXIN VI IN A                  
REMARK   1  TITL 2 CALCIUM-BOUND STATE                                          
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1387   103 1998              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1  DOI    10.1016/S0167-4838(98)00111-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 26029                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1270                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4246                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 223                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5264                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 148                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.76                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 8.280 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 13.010; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.260; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 14.990; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1M9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016764.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.971                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32036                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: HUMAN ANNEXIN VI                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M AMMONIUM SULFATE, 0.1M              
REMARK 280  IMIDAZOLE, PH 7.4, VAPOR DIFFUSION, TEMPERATURE 298.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.30000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      153.45000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.15000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  CA    CA  A   705     O    HOH A   706              0.45            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  14       98.75    -63.29                                   
REMARK 500    HIS A  15      137.18    -30.11                                   
REMARK 500    ASP A  16       77.75    -67.10                                   
REMARK 500    PHE A  17      145.64     67.59                                   
REMARK 500    PHE A  20     -166.30   -102.30                                   
REMARK 500    GLU A  83      -70.14    -54.16                                   
REMARK 500    ASP A 170     -105.42    173.36                                   
REMARK 500    VAL A 171      103.82    -45.93                                   
REMARK 500    GLU A 189      -51.86    -27.54                                   
REMARK 500    LEU A 190        3.12    -68.81                                   
REMARK 500    LEU A 234     -147.97   -113.56                                   
REMARK 500    SER A 251       97.31    179.90                                   
REMARK 500    LYS A 265      -78.54    -14.35                                   
REMARK 500    ARG A 270       58.86   -104.27                                   
REMARK 500    LEU A 284      -70.21   -125.56                                   
REMARK 500    ASP A 285       27.07   -142.73                                   
REMARK 500    GLU A 298       47.68     33.36                                   
REMARK 500    LYS A 299      108.58   -176.14                                   
REMARK 500    SER A 300      147.53    -25.50                                   
REMARK 500    ASP A 324       10.34    178.64                                   
REMARK 500    ASP A 325       84.40    -61.34                                   
REMARK 500    ALA A 327     -146.50     55.20                                   
REMARK 500    ALA A 328      -76.93    -74.47                                   
REMARK 500    LYS A 377      109.16    -50.56                                   
REMARK 500    LYS A 483      161.34    176.74                                   
REMARK 500    GLU A 514     -118.93    -39.93                                   
REMARK 500    ASN A 515       96.77    112.42                                   
REMARK 500    LEU A 530      -71.21   -104.22                                   
REMARK 500    ILE A 532       57.92   -140.60                                   
REMARK 500    ALA A 533     -137.89    -82.99                                   
REMARK 500    ASP A 534     -148.51     52.69                                   
REMARK 500    PRO A 536       30.19    -77.59                                   
REMARK 500    ASP A 539       92.41    -55.88                                   
REMARK 500    LYS A 540       28.92    -74.99                                   
REMARK 500    THR A 541     -109.28     62.28                                   
REMARK 500    GLU A 544     -175.59     49.99                                   
REMARK 500    MET A 569     -153.22    -73.40                                   
REMARK 500    THR A 570       92.92    -19.62                                   
REMARK 500    ASN A 571       24.25    -37.52                                   
REMARK 500    LYS A 580      -72.74    -74.64                                   
REMARK 500    ASN A 599       84.54   -156.21                                   
REMARK 500    ALA A 615      -83.24    -72.95                                   
REMARK 500    ILE A 632      -72.54   -122.56                                   
REMARK 500    ASP A 646       19.12     47.13                                   
REMARK 500    GLU A 672      -88.45     24.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A 376   O                                                      
REMARK 620 2 GLY A 378   O    74.7                                              
REMARK 620 3 LEU A 379   O   131.0  64.2                                        
REMARK 620 4 GLY A 380   O   100.1  87.6  54.5                                  
REMARK 620 5 GLU A 420   OE1  82.6  97.7 126.9 174.5                            
REMARK 620 6 GLU A 420   OE2 107.1 152.7 121.8 118.1  56.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 308   OD2                                                    
REMARK 620 2 MET A 264   O   122.0                                              
REMARK 620 3 GLY A 266   O   125.3  90.2                                        
REMARK 620 4 GLY A 268   O    84.3 140.4  97.4                                  
REMARK 620 5 ASP A 308   OD1  43.3  82.0 149.7 107.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 703  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 770   O                                                      
REMARK 620 2 ASP A 656   OD1  87.8                                              
REMARK 620 3 MET A 612   O   143.8  72.0                                        
REMARK 620 4 GLY A 616   O   103.0 102.0 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 704  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 452   O                                                      
REMARK 620 2 MET A 448   O   127.6                                              
REMARK 620 3 GLY A 450   N   125.5  78.3                                        
REMARK 620 4 ASP A 492   OD1  84.9  76.3 148.7                                  
REMARK 620 5 GLY A 450   O    88.8 132.7  54.6 144.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 705  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  37   O                                                      
REMARK 620 2 MET A  33   O   107.6                                              
REMARK 620 3 GLU A  77   OE1  75.5  88.9                                        
REMARK 620 4 GLY A  35   O   101.8 121.6 147.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 703                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 704                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 705                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AVC   RELATED DB: PDB                                   
REMARK 900 1AVC IS THE NATIVE BOVINE STRUCTURE (CALCIUM-BOUND)                  
DBREF  1M9I A    2   673  UNP    P08133   ANXA6_HUMAN      1    672             
SEQADV 1M9I ASP A  356  UNP  P08133    THR   355 ENGINEERED                     
SEQADV 1M9I ASP A  619  UNP  P08133    GLU   618 SEE REMARK 999                 
SEQRES   1 A  672  ALA LYS PRO ALA GLN GLY ALA LYS TYR ARG GLY SER ILE          
SEQRES   2 A  672  HIS ASP PHE PRO GLY PHE ASP PRO ASN GLN ASP ALA GLU          
SEQRES   3 A  672  ALA LEU TYR THR ALA MET LYS GLY PHE GLY SER ASP LYS          
SEQRES   4 A  672  GLU ALA ILE LEU ASP ILE ILE THR SER ARG SER ASN ARG          
SEQRES   5 A  672  GLN ARG GLN GLU VAL CYS GLN SER TYR LYS SER LEU TYR          
SEQRES   6 A  672  GLY LYS ASP LEU ILE ALA ASP LEU LYS TYR GLU LEU THR          
SEQRES   7 A  672  GLY LYS PHE GLU ARG LEU ILE VAL GLY LEU MET ARG PRO          
SEQRES   8 A  672  PRO ALA TYR CYS ASP ALA LYS GLU ILE LYS ASP ALA ILE          
SEQRES   9 A  672  SER GLY ILE GLY THR ASP GLU LYS CYS LEU ILE GLU ILE          
SEQRES  10 A  672  LEU ALA SER ARG THR ASN GLU GLN MET HIS GLN LEU VAL          
SEQRES  11 A  672  ALA ALA TYR LYS ASP ALA TYR GLU ARG ASP LEU GLU ALA          
SEQRES  12 A  672  ASP ILE ILE GLY ASP THR SER GLY HIS PHE GLN LYS MET          
SEQRES  13 A  672  LEU VAL VAL LEU LEU GLN GLY THR ARG GLU GLU ASP ASP          
SEQRES  14 A  672  VAL VAL SER GLU ASP LEU VAL GLN GLN ASP VAL GLN ASP          
SEQRES  15 A  672  LEU TYR GLU ALA GLY GLU LEU LYS TRP GLY THR ASP GLU          
SEQRES  16 A  672  ALA GLN PHE ILE TYR ILE LEU GLY ASN ARG SER LYS GLN          
SEQRES  17 A  672  HIS LEU ARG LEU VAL PHE ASP GLU TYR LEU LYS THR THR          
SEQRES  18 A  672  GLY LYS PRO ILE GLU ALA SER ILE ARG GLY GLU LEU SER          
SEQRES  19 A  672  GLY ASP PHE GLU LYS LEU MET LEU ALA VAL VAL LYS CYS          
SEQRES  20 A  672  ILE ARG SER THR PRO GLU TYR PHE ALA GLU ARG LEU PHE          
SEQRES  21 A  672  LYS ALA MET LYS GLY LEU GLY THR ARG ASP ASN THR LEU          
SEQRES  22 A  672  ILE ARG ILE MET VAL SER ARG SER GLU LEU ASP MET LEU          
SEQRES  23 A  672  ASP ILE ARG GLU ILE PHE ARG THR LYS TYR GLU LYS SER          
SEQRES  24 A  672  LEU TYR SER MET ILE LYS ASN ASP THR SER GLY GLU TYR          
SEQRES  25 A  672  LYS LYS THR LEU LEU LYS LEU SER GLY GLY ASP ASP ASP          
SEQRES  26 A  672  ALA ALA GLY GLN PHE PHE PRO GLU ALA ALA GLN VAL ALA          
SEQRES  27 A  672  TYR GLN MET TRP GLU LEU SER ALA VAL ALA ARG VAL GLU          
SEQRES  28 A  672  LEU LYS GLY ASP VAL ARG PRO ALA ASN ASP PHE ASN PRO          
SEQRES  29 A  672  ASP ALA ASP ALA LYS ALA LEU ARG LYS ALA MET LYS GLY          
SEQRES  30 A  672  LEU GLY THR ASP GLU ASP THR ILE ILE ASP ILE ILE THR          
SEQRES  31 A  672  HIS ARG SER ASN VAL GLN ARG GLN GLN ILE ARG GLN THR          
SEQRES  32 A  672  PHE LYS SER HIS PHE GLY ARG ASP LEU MET THR ASP LEU          
SEQRES  33 A  672  LYS SER GLU ILE SER GLY ASP LEU ALA ARG LEU ILE LEU          
SEQRES  34 A  672  GLY LEU MET MET PRO PRO ALA HIS TYR ASP ALA LYS GLN          
SEQRES  35 A  672  LEU LYS LYS ALA MET GLU GLY ALA GLY THR ASP GLU LYS          
SEQRES  36 A  672  ALA LEU ILE GLU ILE LEU ALA THR ARG THR ASN ALA GLU          
SEQRES  37 A  672  ILE ARG ALA ILE ASN GLU ALA TYR LYS GLU ASP TYR HIS          
SEQRES  38 A  672  LYS SER LEU GLU ASP ALA LEU SER SER ASP THR SER GLY          
SEQRES  39 A  672  HIS PHE ARG ARG ILE LEU ILE SER LEU ALA THR GLY HIS          
SEQRES  40 A  672  ARG GLU GLU GLY GLY GLU ASN LEU ASP GLN ALA ARG GLU          
SEQRES  41 A  672  ASP ALA GLN VAL ALA ALA GLU ILE LEU GLU ILE ALA ASP          
SEQRES  42 A  672  THR PRO SER GLY ASP LYS THR SER LEU GLU THR ARG PHE          
SEQRES  43 A  672  MET THR ILE LEU CYS THR ARG SER TYR PRO HIS LEU ARG          
SEQRES  44 A  672  ARG VAL PHE GLN GLU PHE ILE LYS MET THR ASN TYR ASP          
SEQRES  45 A  672  VAL GLU HIS THR ILE LYS LYS GLU MET SER GLY ASP VAL          
SEQRES  46 A  672  ARG ASP ALA PHE VAL ALA ILE VAL GLN SER VAL LYS ASN          
SEQRES  47 A  672  LYS PRO LEU PHE PHE ALA ASP LYS LEU TYR LYS SER MET          
SEQRES  48 A  672  LYS GLY ALA GLY THR ASP ASP LYS THR LEU THR ARG ILE          
SEQRES  49 A  672  MET VAL SER ARG SER GLU ILE ASP LEU LEU ASN ILE ARG          
SEQRES  50 A  672  ARG GLU PHE ILE GLU LYS TYR ASP LYS SER LEU HIS GLN          
SEQRES  51 A  672  ALA ILE GLU GLY ASP THR SER GLY ASP PHE LEU LYS ALA          
SEQRES  52 A  672  LEU LEU ALA LEU CYS GLY GLY GLU ASP                          
HET     CA  A 701       1                                                       
HET     CA  A 702       1                                                       
HET     CA  A 703       1                                                       
HET     CA  A 704       1                                                       
HET     CA  A 705       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    5(CA 2+)                                                     
FORMUL   7  HOH   *148(H2 O)                                                    
HELIX    1   1 ASP A   21  MET A   33  1                                  13    
HELIX    2   2 ASP A   39  THR A   48  1                                  10    
HELIX    3   3 SER A   51  GLY A   67  1                                  17    
HELIX    4   4 ASP A   69  LEU A   78  1                                  10    
HELIX    5   5 THR A   79  ARG A   91  1                                  13    
HELIX    6   6 PRO A   92  SER A  106  1                                  15    
HELIX    7   7 ASP A  111  ARG A  122  1                                  12    
HELIX    8   8 THR A  123  TYR A  138  1                                  16    
HELIX    9   9 ASP A  141  THR A  150  1                                  10    
HELIX   10  10 SER A  151  GLY A  164  1                                  14    
HELIX   11  11 SER A  173  GLY A  188  1                                  16    
HELIX   12  12 ASP A  195  ARG A  206  1                                  12    
HELIX   13  13 SER A  207  THR A  222  1                                  16    
HELIX   14  14 PRO A  225  ARG A  231  1                                   7    
HELIX   15  15 SER A  235  ALA A  263  1                                  29    
HELIX   16  16 ARG A  270  ARG A  281  1                                  12    
HELIX   17  17 ASP A  285  TYR A  297  1                                  13    
HELIX   18  18 SER A  300  ASN A  307  1                                   8    
HELIX   19  19 SER A  310  GLY A  322  1                                  13    
HELIX   20  20 PHE A  332  ALA A  349  1                                  18    
HELIX   21  21 ASN A  364  LYS A  377  1                                  14    
HELIX   22  22 ASP A  382  HIS A  392  1                                  11    
HELIX   23  23 SER A  394  GLY A  410  1                                  17    
HELIX   24  24 ASP A  412  ILE A  421  1                                  10    
HELIX   25  25 GLY A  423  MET A  434  1                                  12    
HELIX   26  26 PRO A  435  GLU A  449  1                                  15    
HELIX   27  27 ASP A  454  ARG A  465  1                                  12    
HELIX   28  28 THR A  466  HIS A  482  1                                  17    
HELIX   29  29 SER A  484  THR A  493  1                                  10    
HELIX   30  30 SER A  494  ALA A  505  1                                  12    
HELIX   31  31 ASN A  515  GLU A  531  1                                  17    
HELIX   32  32 ASP A  534  GLY A  538  5                                   5    
HELIX   33  33 THR A  545  ARG A  554  1                                  10    
HELIX   34  34 SER A  555  MET A  569  1                                  15    
HELIX   35  35 ASP A  573  MET A  582  1                                  10    
HELIX   36  36 SER A  583  MET A  612  1                                  30    
HELIX   37  37 ASP A  618  ARG A  629  1                                  12    
HELIX   38  38 ASP A  633  ASP A  646  1                                  14    
HELIX   39  39 SER A  648  THR A  657  1                                  10    
HELIX   40  40 SER A  658  CYS A  669  1                                  12    
LINK        CA    CA A 701                 O   MET A 376     1555   1555  2.58  
LINK        CA    CA A 701                 O   GLY A 378     1555   1555  2.95  
LINK        CA    CA A 701                 O   LEU A 379     1555   1555  3.33  
LINK        CA    CA A 701                 O   GLY A 380     1555   1555  2.04  
LINK        CA    CA A 701                 OE1 GLU A 420     1555   1555  2.61  
LINK        CA    CA A 701                 OE2 GLU A 420     1555   1555  1.80  
LINK        CA    CA A 702                 OD2 ASP A 308     1555   1555  3.20  
LINK        CA    CA A 702                 O   MET A 264     1555   1555  2.82  
LINK        CA    CA A 702                 O   GLY A 266     1555   1555  2.07  
LINK        CA    CA A 702                 O   GLY A 268     1555   1555  1.61  
LINK        CA    CA A 702                 OD1 ASP A 308     1555   1555  2.28  
LINK        CA    CA A 703                 O   HOH A 770     1555   1555  2.90  
LINK        CA    CA A 703                 OD1 ASP A 656     1555   1555  2.40  
LINK        CA    CA A 703                 O   MET A 612     1555   1555  2.75  
LINK        CA    CA A 703                 O   GLY A 616     1555   1555  2.61  
LINK        CA    CA A 704                 O   GLY A 452     1555   1555  2.77  
LINK        CA    CA A 704                 O   MET A 448     1555   1555  1.60  
LINK        CA    CA A 704                 N   GLY A 450     1555   1555  3.27  
LINK        CA    CA A 704                 OD1 ASP A 492     1555   1555  2.54  
LINK        CA    CA A 704                 O   GLY A 450     1555   1555  1.90  
LINK        CA    CA A 705                 O   GLY A  37     1555   1555  2.79  
LINK        CA    CA A 705                 O   MET A  33     1555   1555  2.41  
LINK        CA    CA A 705                 OE1 GLU A  77     1555   1555  2.72  
LINK        CA    CA A 705                 O   GLY A  35     1555   1555  2.14  
SITE     1 AC1  5 MET A 376  GLY A 378  LEU A 379  GLY A 380                    
SITE     2 AC1  5 GLU A 420                                                     
SITE     1 AC2  4 MET A 264  GLY A 266  GLY A 268  ASP A 308                    
SITE     1 AC3  6 MET A 612  GLY A 614  ALA A 615  GLY A 616                    
SITE     2 AC3  6 ASP A 656  HOH A 770                                          
SITE     1 AC4  5 MET A 448  GLU A 449  GLY A 450  GLY A 452                    
SITE     2 AC4  5 ASP A 492                                                     
SITE     1 AC5  5 MET A  33  LYS A  34  GLY A  35  GLY A  37                    
SITE     2 AC5  5 GLU A  77                                                     
CRYST1   67.970   67.970  204.600  90.00  90.00  90.00 P 43          4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014712  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004888        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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